DCW1_YEAST
ID DCW1_YEAST Reviewed; 449 AA.
AC P36091; D6VXP1; Q66R60;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Mannan endo-1,6-alpha-mannosidase DCW1;
DE EC=3.2.1.101;
DE AltName: Full=Defective cell wall 1;
DE AltName: Full=Endo-alpha-1->6-D-mannanase DCW1;
DE Flags: Precursor;
GN Name=DCW1; OrderedLocusNames=YKL046C; ORFNames=YKL259;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8154189; DOI=10.1002/yea.320091212;
RA Purnelle B., Tettelin H., van Dyck L., Skala J., Goffeau A.;
RT "The sequence of a 17.5 kb DNA fragment on the left arm of yeast chromosome
RT XI identifies the protein kinase gene ELM1, the DNA primase gene PRI2, a
RT new gene encoding a putative histone and seven new open reading frames.";
RL Yeast 9:1379-1384(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=12421307; DOI=10.1046/j.1365-2958.2002.03244.x;
RA Kitagaki H., Wu H., Shimoi H., Ito K.;
RT "Two homologous genes, DCW1 (YKL046c) and DFG5, are essential for cell
RT growth and encode glycosylphosphatidylinositol (GPI)-anchored membrane
RT proteins required for cell wall biogenesis in Saccharomyces cerevisiae.";
RL Mol. Microbiol. 46:1011-1022(2002).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Required for normal synthesis of the cell wall.
CC {ECO:0000269|PubMed:12421307}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random hydrolysis of (1->6)-alpha-D-mannosidic linkages in
CC unbranched (1->6)-mannans.; EC=3.2.1.101;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12421307};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:12421307}. Note=GPI-
CC anchored plasma membrane protein (GPI-PMP).
CC -!- MISCELLANEOUS: Present with 2580 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 76 family. {ECO:0000305}.
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DR EMBL; X71621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z28046; CAA81881.1; -; Genomic_DNA.
DR EMBL; AY723839; AAU09756.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09111.1; -; Genomic_DNA.
DR PIR; S37867; S37867.
DR RefSeq; NP_012878.1; NM_001179612.1.
DR AlphaFoldDB; P36091; -.
DR SMR; P36091; -.
DR BioGRID; 34087; 91.
DR IntAct; P36091; 2.
DR MINT; P36091; -.
DR STRING; 4932.YKL046C; -.
DR CAZy; GH76; Glycoside Hydrolase Family 76.
DR PaxDb; P36091; -.
DR PRIDE; P36091; -.
DR EnsemblFungi; YKL046C_mRNA; YKL046C; YKL046C.
DR GeneID; 853820; -.
DR KEGG; sce:YKL046C; -.
DR SGD; S000001529; DCW1.
DR VEuPathDB; FungiDB:YKL046C; -.
DR eggNOG; ENOG502QSWP; Eukaryota.
DR HOGENOM; CLU_025694_1_2_1; -.
DR InParanoid; P36091; -.
DR OMA; QQSFKGY; -.
DR BioCyc; YEAST:G3O-31847-MON; -.
DR PRO; PR:P36091; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36091; protein.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:SGD.
DR GO; GO:0005933; C:cellular bud; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0008496; F:mannan endo-1,6-alpha-mannosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0007117; P:budding cell bud growth; IGI:SGD.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IDA:SGD.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR005198; Glyco_hydro_76.
DR InterPro; IPR014480; Mannan-1_6-alpha_mannosidase.
DR PANTHER; PTHR12145; PTHR12145; 1.
DR Pfam; PF03663; Glyco_hydro_76; 1.
DR PIRSF; PIRSF016302; Man_a_manosd; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall biogenesis/degradation; Glycoprotein; Glycosidase;
KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..428
FT /note="Mannan endo-1,6-alpha-mannosidase DCW1"
FT /id="PRO_0000012125"
FT PROPEP 429..449
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000012126"
FT LIPID 428
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 276
FT /note="T -> A (in Ref. 4; AAU09756)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 449 AA; 49565 MW; DECFE9CAFD9579D5 CRC64;
MLVNKVIGLL GVLFATRFTN AVELDLDNYE SLQNATSLIA YGLMDYYTGN QYGKTVGMFS
DPYYWWEAGG AWGCMLDYWF FMDNDTYNDE IIAAMIHQAG DDNDYIPLNQ STTEGNDDQA
FWGIAAMTAA ERNFTNPPEN EPQWLYLAQA VFNTMALRWD ADSCGGGLRW QIFVWNSGYD
YKNTVSNGAL FHIAARLARY TGNQTYVDWA EKVYEWMVGV NLISNGTYKY VYDGVSIDDN
CTKVTSYQWT YNQGLLLAGS AYLYNFTGSD LWHTRTKEFL NASQVFFHDG IVYEAACQGP
NSCNTDQRSF KAYFARFLGV TAQLVPETRN QIMSWLNTSA IAAAKSCSGG TDGHTCGLNW
FNGTWDGMYG LGEQMSALEV MVNTRALDKP APYTAENGGS SVGDGAAGTQ AQPTNLAPLN
ITKGSKAGAG IITAVIGISI VACALWLVF
